Interaction of DnaK with ATP: Binding, hydrolysis and Ca+2-stimulated autophosphorylation
The autophosphorylation of DnaK from Escherichia coli using ATP as phosphate donor is markedly stimulated by Ca+2 and to a lesser degree by Mn+2. Mg+2 and other divalent ions are without effect in this reaction. Lanthanum, an agonist/antagonist of Ca+2, is also effective in stimulating the autophosp...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1990-02, Vol.166 (3), p.1284-1292 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Dalie, Barbara L. Skaleris, Diane A. Köhle, Kathrin Weissbach, Herbert Brot, Nathan |
| description | The autophosphorylation of DnaK from Escherichia coli using ATP as phosphate donor is markedly stimulated by Ca+2 and to a lesser degree by Mn+2. Mg+2 and other divalent ions are without effect in this reaction. Lanthanum, an agonist/antagonist of Ca+2, is also effective in stimulating the autophosphorylation. In contrast, Mg+2 but not Ca+2, markedly stimulates the hydrolysis of ATP catalyzed by DnaK. Also at 0°, ATP forms a stable complex with DnaK without hydrolysis that is independent of cations. About 15% of the DnaK in E. coli is associated with membrane vesicles where it also can be phosphorylated in the presence of Ca+2. |
| doi_str_mv | 10.1016/0006-291X(90)91005-D |
| format | Article |
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Mg+2 and other divalent ions are without effect in this reaction. Lanthanum, an agonist/antagonist of Ca+2, is also effective in stimulating the autophosphorylation. In contrast, Mg+2 but not Ca+2, markedly stimulates the hydrolysis of ATP catalyzed by DnaK. Also at 0°, ATP forms a stable complex with DnaK without hydrolysis that is independent of cations. 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Mg+2 and other divalent ions are without effect in this reaction. Lanthanum, an agonist/antagonist of Ca+2, is also effective in stimulating the autophosphorylation. In contrast, Mg+2 but not Ca+2, markedly stimulates the hydrolysis of ATP catalyzed by DnaK. Also at 0°, ATP forms a stable complex with DnaK without hydrolysis that is independent of cations. About 15% of the DnaK in E. coli is associated with membrane vesicles where it also can be phosphorylated in the presence of Ca+2.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Amino Acids - analysis</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biological and medical sciences</subject><subject>Calcium - pharmacology</subject><subject>Cations, Divalent</subject><subject>Cell Membrane - metabolism</subject><subject>Egtazic Acid - pharmacology</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Heat-Shock Proteins - metabolism</subject><subject>HSP70 Heat-Shock Proteins</subject><subject>Hydrolysis</subject><subject>Interactions. 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Psychology</topic><topic>Heat-Shock Proteins - metabolism</topic><topic>HSP70 Heat-Shock Proteins</topic><topic>Hydrolysis</topic><topic>Interactions. Associations</topic><topic>Intermolecular phenomena</topic><topic>Kinetics</topic><topic>Lanthanum - pharmacology</topic><topic>Molecular biophysics</topic><topic>Phosphorylation</topic><topic>Protein Binding</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dalie, Barbara L.</creatorcontrib><creatorcontrib>Skaleris, Diane A.</creatorcontrib><creatorcontrib>Köhle, Kathrin</creatorcontrib><creatorcontrib>Weissbach, Herbert</creatorcontrib><creatorcontrib>Brot, Nathan</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dalie, Barbara L.</au><au>Skaleris, Diane A.</au><au>Köhle, Kathrin</au><au>Weissbach, Herbert</au><au>Brot, Nathan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction of DnaK with ATP: Binding, hydrolysis and Ca+2-stimulated autophosphorylation</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1990-02-14</date><risdate>1990</risdate><volume>166</volume><issue>3</issue><spage>1284</spage><epage>1292</epage><pages>1284-1292</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>The autophosphorylation of DnaK from Escherichia coli using ATP as phosphate donor is markedly stimulated by Ca+2 and to a lesser degree by Mn+2. Mg+2 and other divalent ions are without effect in this reaction. Lanthanum, an agonist/antagonist of Ca+2, is also effective in stimulating the autophosphorylation. In contrast, Mg+2 but not Ca+2, markedly stimulates the hydrolysis of ATP catalyzed by DnaK. Also at 0°, ATP forms a stable complex with DnaK without hydrolysis that is independent of cations. About 15% of the DnaK in E. coli is associated with membrane vesicles where it also can be phosphorylated in the presence of Ca+2.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>2106314</pmid><doi>10.1016/0006-291X(90)91005-D</doi><tpages>9</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1990-02, Vol.166 (3), p.1284-1292 |
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| subjects | Adenosine Triphosphate - metabolism Amino Acids - analysis Bacterial Proteins - metabolism Biological and medical sciences Calcium - pharmacology Cations, Divalent Cell Membrane - metabolism Egtazic Acid - pharmacology Escherichia coli - metabolism Escherichia coli Proteins Fundamental and applied biological sciences. Psychology Heat-Shock Proteins - metabolism HSP70 Heat-Shock Proteins Hydrolysis Interactions. Associations Intermolecular phenomena Kinetics Lanthanum - pharmacology Molecular biophysics Phosphorylation Protein Binding |
| title | Interaction of DnaK with ATP: Binding, hydrolysis and Ca+2-stimulated autophosphorylation |
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